Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.1/4797
Título: Purification and characterization milk-clotting aspartic proteinases from Centaurea calcitrapa cell suspension cultures
Autor: Raposo, Sara
Domingos, Ana
Palavras-chave: Centaurea calcitrapa
Milk-clotting protease
Purification
Aspartic proteinases
Plant cell culture
Cell suspension
Data: 2008
Editora: Elsevier
Citação: Raposo, Sara; Domingos, Ana. Purification and characterization milk-clotting aspartic proteinases from Centaurea calcitrapa cell suspension cultures, Process Biochemistry, 43, 2, 139-144, 2008.
Resumo: Plant aspartic proteinases (APs) were isolated from several sources and studied for milk-clotting ability. Extraction of milk-clotting proteinases from intact plants is labor intensive and so, plant cell cultures is a viable alternative to obtain clotting enzymes. The aim of this work was to isolate APs from established suspension cell cultures of Centaurea calcitrapa and evaluate it's the potential interest for milk clotting. Plant cell extract was purified by ionic-exchange and hydrophobic-interaction chromatographies. Results suggest that the milk-clotting proteinases from cell cultures are synthesized as a 66-kDa proenzyme which originates a 50-kDa mature enzyme. The enzyme inhibition of 92% by pepstatin at 10 μM proved it to be an aspartate proteinase. The clotting time for purified APs suggests that these extracts may be used in the production of dairy products of weak paste or conjugated with other commercial rennets.
Peer review: yes
URI: http://hdl.handle.net/10400.1/4797
DOI: http://dx.doi.org/ 10.1016/j.procbio.2007.11.003
ISSN: 1359-5113
Versão do Editor: http://www.sciencedirect.com/science/article/pii/S1359511307003030
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